Subunits of alpha-crystallin from bovine lenses will be isolated and purified. Their hydration property alone and in combination of two and three kinds of subunits will be studied. Phosphopeptides causing crystallin organization of macromolecules in isoelectrically precipitated alpha-crystallin fraction of bovine lens will be characterized regarding amino acid composition and sequence. It will be studied which subunit of alpha-crystallin or other component of the precipitated mixture is responsible for the interaction with these phosphopeptides. Light scattering patterns of human and rat cornea will be interpreted in terms of a model of two dimensional non-random assembly of anisotropic rods. The dynamic light scattering patterns obtained during vibrational cycles of bovine cornea will also be interpreted with the above model. Birefringence studies on vitreous and in a number of acidid polysaccharide films will be conducted.